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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Almeida, D.
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Publications (2/2 displayed)
- 2020Characterization of planktonic and biofilm cells from two filamentous cyanobacteria using a shotgun proteomic approachcitations
- 2015Electronic excitation of carbonyl sulphide (COS) by high-resolution vacuum ultraviolet photoabsorption and electron-impact spectroscopy in the energy region from 4 to 11 eVcitations
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article
Characterization of planktonic and biofilm cells from two filamentous cyanobacteria using a shotgun proteomic approach
Abstract
Cyanobacteria promote marine biofouling with significant impacts. A qualitative proteomic analysis, by LC-MS/MS, of planktonic and biofilm cells from two cyanobacteria was performed. Biofilms were formed on glass and perspex at two relevant hydrodynamic conditions for marine environments (average shear rates of 4 s(-1)and 40 s(-1)). For both strains and surfaces, biofilm development was higher at 4 s(-1). Biofilm development ofNodosilineasp. LEGE 06145 was substantially higher thanNodosilineasp. LEGE 06119, but no significant differences were found between surfaces. Overall, 377 and 301 different proteins were identified forNodosilineasp. LEGE 06145 andNodosilineasp. LEGE 06119. Differences in protein composition were more noticeable in biofilms formed under different hydrodynamic conditions than in those formed on different surfaces. Ribosomal and photosynthetic proteins were identified in most conditions. The characterization performed gives new insights into how shear rate and surface affect the planktonic to biofilm transition, from a structural and proteomics perspective.